My research focuses on utilising synthetic biology to scrutinize the assembly, metabolic regulation and kinetic plasticity of the biospheres most abundant protein, the photosynthetic CO₂-fixing enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The research provides training in molecular biology, protein engineering (directed evolution), enzyme kinetics, biochemistry, plastome transformation, tissue culture, measuring leaf photosynthesis and plant growth.

Despites Rubisco’s pivotal role in photosynthetic carbon assimilation – catalysing the primary step of incorporating CO₂ into carbohydrates that are used to store and transport energy - it is surprisingly an inefficient enzyme in need of improvement. It constitutes about 20 to 30% of soluble leaf protein due to its inefficiency. The catalytic inadequacies of Rubisco (such as a slow turnover rate and poor ability to distinguish CO₂ from O₂) frequently limit the growth capacity of many plants, including most crops. As such, Rubisco has been studied intensively as a prime target for genetic engineering as a means to supercharge photosynthesis and improve growth efficiency. Towards this significant challenge, the primary foci of research in the Whitney laboratory utilises recent technological and conceptual breakthroughs to study Rubisco biogenesis, modify its catalysis, understand its regulation by Rubisco activase and generally tackle the challenges faced in developing strategies for enhancing Rubisco activity to improve plant productivity.